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Literature summary extracted from

  • Trainer, M.A.; Capstick, D.; Zachertowska, A.; Lam, K.N.; Clark, S.R.; Charles, T.C.
    Identification and characterization of the intracellular poly-3-hydroxybutyrate depolymerase enzyme PhaZ of Sinorhizobium meliloti (2010), BMC Microbiol., 10, 92.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.1.1.75 expressed in Escherichia coli as a His-tagged fusion protein Sinorhizobium meliloti

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.1.1.75 intracellular
-
 Sinorhizobium meliloti 5622
-

Organism

EC Number Organism UniProt Comment Textmining
3.1.1.75 Sinorhizobium meliloti
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.1.75 poly-3-hydroxybutyrate + H2O
-
 Sinorhizobium meliloti ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.1.1.75 PhaZ
-
 Sinorhizobium meliloti
3.1.1.75 poly(3-hydroxybutyrate) depolymerase
-
 Sinorhizobium meliloti

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.1.1.75 30
-
 assay at Sinorhizobium meliloti

General Information

EC Number General Information Comment Organism
3.1.1.75 malfunction a phaZ mutant exhibits increased poly-3-hydroxybutyrate accumulation during free-living growth, even when grown under non-poly-3-hydroxybutyrate -inducing conditions. The phaZ mutant demonstrates no reduction in symbiotic capacity. This mutant also exhibits a decreased capacity to tolerate long-term carbon starvation, comparable to that of other poly-3-hydroxybutyrate cycle mutants. In contrast to other poly-3-hydroxybutyrate cycle mutants, the phaZ mutant does not exhibit any decrease in rhizosphere competitiveness, but it exhibits a significant increase in succinoglycan biosynthesis Sinorhizobium meliloti